Acceleration effect of sericin on shear-induced β-transition of silk fibroin

Chang Seok Ki, In Chul Um, Young Hwan Park

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


Although silk sericin (SS) occupies 25% of silk protein, its importance has often been overlooked in the natural silk spinning process and in the formation of the crystalline structure of silk fibroin (SF). In this study, we elucidated the role of SS in the crystallization process of SF under shear using SF/SS blend solutions. In order to apply shear stress to the blend solution, a rotating glass rod was inserted into a glass tube filled with the solution and the shear rate was determined to be in the range of 598-724 s-1. After shearing, SF aggregates were formed and the amount of the aggregates increased with shearing time. Additionally, it was observed that the aggregate formation and β-sheet transition of SF were enhanced when a proper amount of SS was in the blend solution. Consequently, the SS considerably contributes to the structural transition of SF under shear. The SS can improve the shear-induced β-sheet transition and crystallization of SF.

Original languageEnglish
Pages (from-to)4618-4625
Number of pages8
Issue number19
StatePublished - 10 Sep 2009


  • Fibroin
  • Sericin
  • β-Transition


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